2IXH
RmlC P aeruginosa with dTDP-rhamnose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0005829 | cellular_component | cytosol |
A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
B | 0000271 | biological_process | polysaccharide biosynthetic process |
B | 0005829 | cellular_component | cytosol |
B | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
B | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TRH A1185 |
Chain | Residue |
A | PHE22 |
A | TYR134 |
A | TRP140 |
A | LYS170 |
A | HOH2229 |
A | HOH2253 |
A | HOH2281 |
A | HOH2282 |
A | HOH2283 |
A | HOH2284 |
A | HOH2285 |
A | ARG26 |
A | HOH2286 |
A | HOH2287 |
A | HOH2288 |
A | PHE29 |
A | GLU31 |
A | GLN50 |
A | ARG62 |
A | HIS65 |
A | LYS74 |
A | HIS121 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TRH B1185 |
Chain | Residue |
B | PHE22 |
B | ARG26 |
B | PHE29 |
B | GLU31 |
B | GLN50 |
B | ARG62 |
B | HIS65 |
B | LYS74 |
B | HIS121 |
B | TYR134 |
B | TRP140 |
B | LYS170 |
B | HOH2272 |
B | HOH2293 |
B | HOH2294 |
B | HOH2295 |
B | HOH2296 |
B | HOH2297 |
B | HOH2298 |
B | HOH2299 |
B | HOH2300 |
B | HOH2301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IXI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Site: {"description":"Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose","evidences":[{"source":"UniProtKB","id":"Q5SFD1","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
A | HIS65 | |
A | ASP171 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dzr |
Chain | Residue | Details |
B | HIS65 | |
B | ASP171 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 329 |
Chain | Residue | Details |
A | HIS65 | proton acceptor, proton donor |
A | LYS74 | electrostatic stabiliser |
A | TYR134 | proton acceptor, proton donor, proton relay |
A | ASP171 | electrostatic stabiliser, increase acidity, increase basicity |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 329 |
Chain | Residue | Details |
B | HIS65 | proton acceptor, proton donor |
B | LYS74 | electrostatic stabiliser |
B | TYR134 | proton acceptor, proton donor, proton relay |
B | ASP171 | electrostatic stabiliser, increase acidity, increase basicity |